narH

Functionⁱ

The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The beta chain is an electron transfer unit containing four cysteine clusters involved in the formation of iron-sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit.

Catalytic activityⁱ

Nitrate + a quinol = nitrite + a quinone + H₂O.

Cofactorⁱ

Protein has several cofactor binding sites:

[4Fe-4S] cluster
2 Publications
Manual assertion based on experiment inⁱ
- Ref.13
  "Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A."
  Bertero M.G., Rothery R.A., Palak M., Hou C., Lim D., Blasco F., Weiner J.H., Strynadka N.C.J.
  Nat. Struct. Biol. 10:681-687(2003) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (3FE-4S) AND IRON-SULFUR (4FE-4S), COFACTOR, SUBUNIT.
- Ref.14
  "Architecture of NarGH reveals a structural classification of Mo-bisMGD enzymes."
  Jormakka M., Richardson D., Byrne B., Iwata S.
  Structure 12:95-104(2004) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (3FE-4S) AND IRON-SULFUR (4FE-4S), COFACTOR.
Note: Binds 3 [4Fe-4S] clusters per subunit.
2 Publications
Manual assertion based on experiment inⁱ
- Ref.13
  "Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A."
  Bertero M.G., Rothery R.A., Palak M., Hou C., Lim D., Blasco F., Weiner J.H., Strynadka N.C.J.
  Nat. Struct. Biol. 10:681-687(2003) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (3FE-4S) AND IRON-SULFUR (4FE-4S), COFACTOR, SUBUNIT.
- Ref.14
  "Architecture of NarGH reveals a structural classification of Mo-bisMGD enzymes."
  Jormakka M., Richardson D., Byrne B., Iwata S.
  Structure 12:95-104(2004) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (3FE-4S) AND IRON-SULFUR (4FE-4S), COFACTOR.
[3Fe-4S] cluster
2 Publications
Manual assertion based on experiment inⁱ
- Ref.13
  "Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A."
  Bertero M.G., Rothery R.A., Palak M., Hou C., Lim D., Blasco F., Weiner J.H., Strynadka N.C.J.
  Nat. Struct. Biol. 10:681-687(2003) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (3FE-4S) AND IRON-SULFUR (4FE-4S), COFACTOR, SUBUNIT.
- Ref.14
  "Architecture of NarGH reveals a structural classification of Mo-bisMGD enzymes."
  Jormakka M., Richardson D., Byrne B., Iwata S.
  Structure 12:95-104(2004) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (3FE-4S) AND IRON-SULFUR (4FE-4S), COFACTOR.
Note: Binds 1 [3Fe-4S] cluster per subunit.
2 Publications
Manual assertion based on experiment inⁱ
- Ref.13
  "Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A."
  Bertero M.G., Rothery R.A., Palak M., Hou C., Lim D., Blasco F., Weiner J.H., Strynadka N.C.J.
  Nat. Struct. Biol. 10:681-687(2003) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (3FE-4S) AND IRON-SULFUR (4FE-4S), COFACTOR, SUBUNIT.
- Ref.14
  "Architecture of NarGH reveals a structural classification of Mo-bisMGD enzymes."
  Jormakka M., Richardson D., Byrne B., Iwata S.
  Structure 12:95-104(2004) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (3FE-4S) AND IRON-SULFUR (4FE-4S), COFACTOR.

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	16	Iron-sulfur 1 (4Fe-4S)2 Publications	1
Metal bindingⁱ	19	Iron-sulfur 1 (4Fe-4S)2 Publications	1
Metal bindingⁱ	22	Iron-sulfur 1 (4Fe-4S)2 Publications	1
Metal bindingⁱ	26	Iron-sulfur 2 (4Fe-4S)2 Publications	1
Metal bindingⁱ	184	Iron-sulfur 3 (4Fe-4S)2 Publications	1
Metal bindingⁱ	187	Iron-sulfur 3 (4Fe-4S)2 Publications	1
Metal bindingⁱ	192	Iron-sulfur 3 (4Fe-4S)2 Publications	1
Metal bindingⁱ	196	Iron-sulfur 4 (3Fe-4S)2 Publications	1
Metal bindingⁱ	217	Iron-sulfur 4 (3Fe-4S)2 Publications	1
Metal bindingⁱ	223	Iron-sulfur 4 (3Fe-4S)2 Publications	1
Metal bindingⁱ	227	Iron-sulfur 3 (4Fe-4S)2 Publications	1
Metal bindingⁱ	244	Iron-sulfur 2 (4Fe-4S)2 Publications	1
Metal bindingⁱ	247	Iron-sulfur 2 (4Fe-4S)2 Publications	1
Metal bindingⁱ	259	Iron-sulfur 2 (4Fe-4S)2 Publications	1
Metal bindingⁱ	263	Iron-sulfur 1 (4Fe-4S)2 Publications	1

GO - Molecular functionⁱ

3 iron, 4 sulfur cluster binding
Source: EcoCyc
Inferred from direct assayⁱ
- 2985594
4 iron, 4 sulfur cluster binding
Source: EcoCyc
Inferred from direct assayⁱ
- 2985594
electron transfer activity
Source: EcoCyc
Inferred from direct assayⁱ
- 1321049
metal ion binding Source: UniProtKB-KW
nitrate reductase activity
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 7047497

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

anaerobic respiration
Source: EcoCyc
Inferred from expression patternⁱ
- 2832376
nitrate assimilation Source: UniProtKB-KW
nitrate metabolic process
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 7047497

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Oxidoreductase
Biological process	Electron transport, Nitrate assimilation, Transport
Ligand	3Fe-4S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCycⁱ	EcoCyc:NARH-MONOMER MetaCyc:NARH-MONOMER
BRENDAⁱ	1.7.5.1 2026

Protein family/group databases

TCDBⁱ	5.A.3.1.1 the prokaryotic molybdopterin-containing oxidoreductase (pmo) family

TCDBⁱ

5.A.3.1.1 the prokaryotic molybdopterin-containing oxidoreductase (pmo) family

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Respiratory nitrate reductase 1 beta chain (EC:1.7.5.1) Alternative name(s): Nitrate reductase A subunit beta Quinol-nitrate oxidoreductase subunit beta
Gene namesⁱ	Name:narH Ordered Locus Names:b1225, JW1216
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG10639 narH

EcoGeneⁱ

EG10639 narH

Subcellular locationⁱ

Cell membrane ; Peripheral membrane protein

GO - Cellular componentⁱ

intrinsic component of membrane
Source: EcoCyc
Inferred from direct assayⁱ
- 5996
intrinsic component of the cytoplasmic side of the plasma membrane
Source: EcoCyc
Inferred from direct assayⁱ
- 12910261
membrane
Source: UniProtKB
Inferred from high throughput direct assayⁱ
- 16858726
NarGHI complex
Source: EcoCyc
Inferred from direct assayⁱ
- 12910261
- 4151408

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cell membrane, Membrane

Pathology & Biotechⁱ

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB04464 N-Formylmethionine

DrugBankⁱ

DB04464 N-Formylmethionine

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000096720	1 – 512	Respiratory nitrate reductase 1 beta chainAdd BLAST		512

Proteomic databases

PaxDbⁱ	P11349
PRIDEⁱ	P11349

Expressionⁱ

Inductionⁱ

By nitrate.

Interactionⁱ

Subunit structureⁱ

Dimer of heterotrimers each composed of an alpha, a beta and a gamma chain. Alpha and beta are catalytic chains; gamma chains are involved in binding the enzyme complex to the cytoplasmic membrane.1 Publication

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
fadH	P42593	3	EBI-555067,EBI-561933
narG	P09152	13	EBI-555067,EBI-547248
narW	P19317	3	EBI-555067,EBI-555088
narY	P19318	3	EBI-555067,EBI-555059
narZ	P19319	6	EBI-555067,EBI-547262

Protein-protein interaction databases

BioGridⁱ	4262231, 28 interactors
ComplexPortalⁱ	CPX-1974 Nitrate reductase A complex
Database of interacting proteins More...DIPⁱ	DIP-10312N
IntActⁱ	P11349, 15 interactors
STRINGⁱ	316385.ECDH10B_1284

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	3 – 12	Combined sources	10
Turnⁱ	13 – 15	Combined sources	3
Helixⁱ	21 – 30	Combined sources	10
Beta strandⁱ	41 – 49	Combined sources	9
Turnⁱ	51 – 57	Combined sources	7
Helixⁱ	59 – 62	Combined sources	4
Beta strandⁱ	65 – 68	Combined sources	4
Beta strandⁱ	74 – 76	Combined sources	3
Helixⁱ	81 – 85	Combined sources	5
Turnⁱ	86 – 89	Combined sources	4
Helixⁱ	97 – 100	Combined sources	4
Beta strandⁱ	104 – 106	Combined sources	3
Helixⁱ	109 – 113	Combined sources	5
Beta strandⁱ	126 – 128	Combined sources	3
Turnⁱ	129 – 131	Combined sources	3
Turnⁱ	142 – 148	Combined sources	7
Helixⁱ	152 – 155	Combined sources	4
Helixⁱ	159 – 161	Combined sources	3
Helixⁱ	167 – 170	Combined sources	4
Helixⁱ	172 – 174	Combined sources	3
Beta strandⁱ	178 – 182	Combined sources	5
Helixⁱ	191 – 194	Combined sources	4
Beta strandⁱ	201 – 204	Combined sources	4
Turnⁱ	205 – 207	Combined sources	3
Beta strandⁱ	210 – 212	Combined sources	3
Turnⁱ	214 – 216	Combined sources	3
Helixⁱ	223 – 226	Combined sources	4
Beta strandⁱ	232 – 235	Combined sources	4
Turnⁱ	236 – 239	Combined sources	4
Beta strandⁱ	240 – 243	Combined sources	4
Helixⁱ	248 – 251	Combined sources	4
Turnⁱ	252 – 254	Combined sources	3
Helixⁱ	258 – 261	Combined sources	4
Beta strandⁱ	268 – 276	Combined sources	9
Helixⁱ	277 – 279	Combined sources	3
Helixⁱ	280 – 284	Combined sources	5
Helixⁱ	289 – 291	Combined sources	3
Helixⁱ	292 – 297	Combined sources	6
Helixⁱ	306 – 314	Combined sources	9
Helixⁱ	319 – 325	Combined sources	7
Helixⁱ	329 – 334	Combined sources	6
Beta strandⁱ	341 – 343	Combined sources	3
Helixⁱ	345 – 347	Combined sources	3
Beta strandⁱ	352 – 356	Combined sources	5
Beta strandⁱ	366 – 368	Combined sources	3
Helixⁱ	380 – 382	Combined sources	3
Beta strandⁱ	383 – 385	Combined sources	3
Helixⁱ	387 – 394	Combined sources	8
Helixⁱ	399 – 420	Combined sources	22
Helixⁱ	428 – 432	Combined sources	5
Helixⁱ	437 – 447	Combined sources	11
Helixⁱ	452 – 455	Combined sources	4
Turnⁱ	463 – 466	Combined sources	4
Helixⁱ	469 – 475	Combined sources	7

Show more details

3D structure databases

ProteinModelPortalⁱ	P11349
SMRⁱ	P11349
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P11349

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	7 – 35	4Fe-4S ferredoxin-type 1PROSITE-ProRule annotationAdd BLAST	29
Domainⁱ	175 – 206	4Fe-4S ferredoxin-type 2PROSITE-ProRule annotationAdd BLAST	32
Domainⁱ	208 – 237	4Fe-4S ferredoxin-type 3PROSITE-ProRule annotationAdd BLAST	30

Keywords - Domainⁱ

Repeat

Phylogenomic databases

eggNOGⁱ	ENOG4108IUE Bacteria COG1140 LUCA
HOGENOMⁱ	HOG000237353
InParanoidⁱ	P11349
KEGG Orthology (KO) More...KOⁱ	K00371
PhylomeDBⁱ	P11349

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd10557 NarH_beta-like, 1 hit
Gene3Dⁱ	1.10.3650.10, 1 hit
InterProⁱ	View protein in InterPro IPR017896 4Fe4S_Fe-S-bd IPR029263 Nitr_red_bet_C IPR038262 Nitr_red_bet_C_sf IPR006547 NO3_Rdtase_bsu
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF13247 Fer4_11, 1 hit PF14711 Nitr_red_bet_C, 1 hit
TIGRFAMsⁱ	TIGR01660 narH, 1 hit
PROSITEⁱ	View protein in PROSITE PS51379 4FE4S_FER_2, 3 hits

Sequenceⁱ

Sequence statusⁱ: Complete.

P11349-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MKIRSQVGMV LNLDKCIGCH TCSVTCKNVW TSREGVEYAW FNNVETKPGQ 
        60         70         80         90        100
GFPTDWENQE KYKGGWIRKI NGKLQPRMGN RAMLLGKIFA NPHLPGIDDY 
       110        120        130        140        150
YEPFDFDYQN LHTAPEGSKS QPIARPRSLI TGERMAKIEK GPNWEDDLGG 
       160        170        180        190        200
EFDKLAKDKN FDNIQKAMYS QFENTFMMYL PRLCEHCLNP ACVATCPSGA 
       210        220        230        240        250
IYKREEDGIV LIDQDKCRGW RMCITGCPYK KIYFNWKSGK SEKCIFCYPR 
       260        270        280        290        300
IEAGQPTVCS ETCVGRIRYL GVLLYDADAI ERAASTENEK DLYQRQLDVF 
       310        320        330        340        350
LDPNDPKVIE QAIKDGIPLS VIEAAQQSPV YKMAMEWKLA LPLHPEYRTL 
       360        370        380        390        400
PMVWYVPPLS PIQSAADAGE LGSNGILPDV ESLRIPVQYL ANLLTAGDTK 
       410        420        430        440        450
PVLRALKRML AMRHYKRAET VDGKVDTRAL EEVGLTEAQA QEMYRYLAIA 
       460        470        480        490        500
NYEDRFVVPS SHRELAREAF PEKNGCGFTF GDGCHGSDTK FNLFNSRRID 
       510 
AIDVTSKTEP HP

Length:512

Mass (Da):58,066

Last modified:February 1, 1996 - v3

Checksum:ⁱ2E7719C8D078BAEA

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	398 – 417	DTKPV…RHYKR → EYQTGTARTETYAGDASLQT in AAA24195 (PubMed:2832376).CuratedAdd BLAST		20

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M20147 Genomic DNA Translation: AAA24195.1 U00096 Genomic DNA Translation: AAC74309.1 AP009048 Genomic DNA Translation: BAA36095.1 X16181 Genomic DNA Translation: CAA34304.1
PIRⁱ	F64869 RDECNB
NCBI Reference Sequences More...RefSeqⁱ	NP_415743.1, NC_000913.3 WP_000702650.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC74309; AAC74309; b1225 BAA36095; BAA36095; BAA36095
GeneIDⁱ	945780
KEGGⁱ	ecj:JW1216 eco:b1225
PATRICⁱ	fig\|1411691.4.peg.1056

Protein	Similar proteins		Species	Score	Length	Source
P11349	Nitrate reductase subunit beta		Shigella sp.		512	UniRef100_P11349
Respiratory nitrate reductase subunit beta		KLEPN		512
Nitrate reductase, beta subunit		Shigella flexneri 1235-66		512
Nitrate reductase		ECOLX		512
Nitrate reductase 1 subunit beta		SHIFL		512
+80

Protein	Similar proteins		Species	Score	Length	Source
P11349	Respiratory nitrate reductase 1 beta chain		SHIFL		512	UniRef90_P11349
Nitrate reductase subunit beta		Shigella sp.		512
Respiratory nitrate reductase subunit beta		KLEPN		512
Nitrate reductase, beta subunit		Shigella flexneri 1235-66		512
Nitrate reductase		ECOLX		512
+1541

Protein	Similar proteins		Species	Score	Length	Source
P11349	Respiratory nitrate reductase 1 beta chain		SHIFL		512	UniRef50_P11349
Respiratory nitrate reductase 2 beta chain		ECOLI		514
Nitrate reductase subunit beta		Shigella sp.		512
Respiratory nitrate reductase subunit beta		KLEPN		512
Nitrate reductase, beta subunit		Shigella flexneri 1235-66		512
+8536

Cross-referencesⁱ

Web resourcesⁱ

Worthington enzyme manual

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M20147 Genomic DNA Translation: AAA24195.1 U00096 Genomic DNA Translation: AAC74309.1 AP009048 Genomic DNA Translation: BAA36095.1 X16181 Genomic DNA Translation: CAA34304.1
PIRⁱ	F64869 RDECNB
RefSeqⁱ	NP_415743.1, NC_000913.3 WP_000702650.1, NZ_LN832404.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1Q16	X-ray	1.90	B	1-512	[»]
	1R27	X-ray	2.00	B/D	1-512	[»]
	1SIW	X-ray	2.20	B	1-512	[»]
	1Y4Z	X-ray	2.00	B	1-512	[»]
	1Y5I	X-ray	1.90	B	1-512	[»]
	1Y5L	X-ray	2.50	B	1-512	[»]
	1Y5N	X-ray	2.50	B	1-512	[»]
	3EGW	X-ray	1.90	B	1-509	[»]
	3IR5	X-ray	2.30	B	1-512	[»]
	3IR6	X-ray	2.80	B	1-512	[»]
	3IR7	X-ray	2.50	B	1-512	[»]
ProteinModelPortalⁱ	P11349
SMRⁱ	P11349
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4262231, 28 interactors
ComplexPortalⁱ	CPX-1974 Nitrate reductase A complex
DIPⁱ	DIP-10312N
IntActⁱ	P11349, 15 interactors
STRINGⁱ	316385.ECDH10B_1284

Chemistry databases

DrugBankⁱ	DB04464 N-Formylmethionine

DrugBankⁱ

DB04464 N-Formylmethionine

Protein family/group databases

TCDBⁱ	5.A.3.1.1 the prokaryotic molybdopterin-containing oxidoreductase (pmo) family

TCDBⁱ

5.A.3.1.1 the prokaryotic molybdopterin-containing oxidoreductase (pmo) family

Proteomic databases

PaxDbⁱ	P11349
PRIDEⁱ	P11349

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC74309; AAC74309; b1225 BAA36095; BAA36095; BAA36095
GeneIDⁱ	945780
KEGGⁱ	ecj:JW1216 eco:b1225
PATRICⁱ	fig\|1411691.4.peg.1056

Organism-specific databases

EchoBASEⁱ	EB0633
EcoGeneⁱ	EG10639 narH

Phylogenomic databases

eggNOGⁱ	ENOG4108IUE Bacteria COG1140 LUCA
HOGENOMⁱ	HOG000237353
InParanoidⁱ	P11349
KOⁱ	K00371
PhylomeDBⁱ	P11349

Enzyme and pathway databases

BioCycⁱ	EcoCyc:NARH-MONOMER MetaCyc:NARH-MONOMER
BRENDAⁱ	1.7.5.1 2026

Miscellaneous databases

EvolutionaryTraceⁱ	P11349
Protein Ontology More...PROⁱ	PR:P11349

Family and domain databases

CDDⁱ	cd10557 NarH_beta-like, 1 hit
Gene3Dⁱ	1.10.3650.10, 1 hit
InterProⁱ	View protein in InterPro IPR017896 4Fe4S_Fe-S-bd IPR029263 Nitr_red_bet_C IPR038262 Nitr_red_bet_C_sf IPR006547 NO3_Rdtase_bsu
Pfamⁱ	View protein in Pfam PF13247 Fer4_11, 1 hit PF14711 Nitr_red_bet_C, 1 hit
TIGRFAMsⁱ	TIGR01660 narH, 1 hit
PROSITEⁱ	View protein in PROSITE PS51379 4FE4S_FER_2, 3 hits
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	NARH_ECOLI
Accessionⁱ	P11349Primary (citable) accession number: P11349
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
	Last sequence update:	February 1, 1996
	Last modified:	November 7, 2018
	This is version 178 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P11349 (NARH_ECOLI)

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Respiratory nitrate reductase 1 beta chain

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

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<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

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<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ